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Deepmind Technologies Ltd
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Molecular Dynamics Inc
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Thermo Fisher
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Journal: Cureus
Article Title: Interaction Between HAQ-STING Mutation and COPA: Protection Against COPA Syndrome
doi: 10.7759/cureus.82254
Figure Lengend Snippet: The plot provides a visual representation of how well the input sequence aligns with other related sequences across the entire sequence. Except at positions 500 and 1220, a significant portion of the protein has moderate sequence identity. AF2M: AlphaFold2 Multimer
Article Snippet: In the current study,
Techniques: Sequencing
Journal: Cureus
Article Title: Interaction Between HAQ-STING Mutation and COPA: Protection Against COPA Syndrome
doi: 10.7759/cureus.82254
Figure Lengend Snippet: PAE plots assess structural confidence and domain flexibility. Blue (low PAE) indicates high-confidence intra-domain folding; red (high PAE) shows uncertain inter-domain positioning. Diagonal blue regions confirm well-defined COPA and HAQ-STING domains. Off-diagonal red regions reflect flexible or variable inter-domain orientations. Model 1 (rank_1) shows slightly higher structural definition. PAE: Predicted aligned error; AF2M: AlphaFold2 Multimer; STING: Stimulator of interferon genes
Article Snippet: In the current study,
Techniques:
Journal: Cureus
Article Title: Interaction Between HAQ-STING Mutation and COPA: Protection Against COPA Syndrome
doi: 10.7759/cureus.82254
Figure Lengend Snippet: pIDDT scores indicate high local structure confidence (70–90) for most residues, with dips below 50 marking flexible or disordered regions. A black line at position 1220 highlights a domain boundary or interaction site with notable structural variability. pIDDT: Predicted intrinsic distance difference test; AF2M: AlphaFold2 Multimer
Article Snippet: In the current study,
Techniques:
Journal: International Journal of Molecular Sciences
Article Title: A Computational Approach in the Systematic Search of the Interaction Partners of Alternatively Spliced TREM2 Isoforms
doi: 10.3390/ijms25179667
Figure Lengend Snippet: General workflow diagram. In step 1, proteome-wide screening by ProteinPrompt was used to identify the prospective interaction partners for TREM2 isoforms. In step 2, independent modeling by PEPPI was used to validate step 1’s predictions. In step 3, the interaction partners identified in step 1 and validated in step 2 were built into a heterodimeric complex with the corresponding TREM isoform by AlphaFold2 Multimer.
Article Snippet:
Techniques:
Journal: International Journal of Molecular Sciences
Article Title: A Computational Approach in the Systematic Search of the Interaction Partners of Alternatively Spliced TREM2 Isoforms
doi: 10.3390/ijms25179667
Figure Lengend Snippet: AlphaFold2 Multimer visualization of the dimeric complexes formed by TREM2 alternatively spliced isoforms and the newfound interaction partners with part of the interacting interface zoomed in: ( A ) TREM2△exon2 (dark green) and CD9 (orange), ( B ) TREM2△exon4 (dark green) and CD9 (orange), ( C ) TREM2△exon5 (dark green) and CALM (orange)—and structural superposition between canonical TREM2 (red) and the isoforms—( D ) between canonical TREM2 and TREM2△exon2, ( E ) between canonical TREM2 and TREM2△exon4, ( F ) between canonical TREM2 and TREM2△exon5.
Article Snippet:
Techniques:
Journal: International Journal of Molecular Sciences
Article Title: A Computational Approach in the Systematic Search of the Interaction Partners of Alternatively Spliced TREM2 Isoforms
doi: 10.3390/ijms25179667
Figure Lengend Snippet: The interacting interfaces in AlphaFold2 Multimer’s three heterodimeric complexes.
Article Snippet:
Techniques: